RL22_HUMAN
ID RL22_HUMAN Reviewed; 128 AA.
AC P35268; B2R495; Q6IBD1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=60S ribosomal protein L22;
DE AltName: Full=EBER-associated protein;
DE Short=EAP;
DE AltName: Full=Epstein-Barr virus small RNA-associated protein;
DE AltName: Full=Heparin-binding protein HBp15;
DE AltName: Full=Large ribosomal subunit protein eL22 {ECO:0000303|PubMed:24524803};
GN Name=RPL22;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-46 AND 108-125.
RC TISSUE=Placenta;
RX PubMed=1846807; DOI=10.1002/j.1460-2075.1991.tb07968.x;
RA Toczyski D.P.W., Steitz J.A.;
RT "EAP, a highly conserved cellular protein associated with Epstein-Barr
RT virus small RNAs (EBERs).";
RL EMBO J. 10:459-466(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Submandibular gland;
RX PubMed=8135813; DOI=10.1006/bbrc.1994.1286;
RA Fujita Y., Okamoto T., Noshiro M., Kato Y., Takada K., Sato J.D., Ozaki T.,
RA McKeehan W.L., Crabb J.W., Whitney R.G.;
RT "A novel heparin-binding protein, HBp15, is identified as mammalian
RT ribosomal protein L22.";
RL Biochem. Biophys. Res. Commun. 199:706-713(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 2-10; 53-65; 70-81 AND 102-113, CLEAVAGE OF INITIATOR
RP METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Cervix, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
RN [16] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
CC -!- FUNCTION: Component of the large ribosomal subunit (PubMed:23636399,
CC PubMed:32669547). The ribosome is a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell (PubMed:23636399,
CC PubMed:32669547). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}.
CC -!- INTERACTION:
CC P35268; Q96CW1: AP2M1; NbExp=3; IntAct=EBI-354533, EBI-297683;
CC P35268; P54253: ATXN1; NbExp=3; IntAct=EBI-354533, EBI-930964;
CC P35268; Q8N7W2-2: BEND7; NbExp=5; IntAct=EBI-354533, EBI-10181188;
CC P35268; Q5HYN5: CT45A1; NbExp=3; IntAct=EBI-354533, EBI-12051833;
CC P35268; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-354533, EBI-742054;
CC P35268; Q92914: FGF11; NbExp=3; IntAct=EBI-354533, EBI-11987787;
CC P35268; U3KQK0: H2BC15; NbExp=3; IntAct=EBI-354533, EBI-12142839;
CC P35268; P42858: HTT; NbExp=3; IntAct=EBI-354533, EBI-466029;
CC P35268; P35268: RPL22; NbExp=3; IntAct=EBI-354533, EBI-354533;
CC P35268; O00560: SDCBP; NbExp=5; IntAct=EBI-354533, EBI-727004;
CC P35268; Q9H190: SDCBP2; NbExp=5; IntAct=EBI-354533, EBI-742426;
CC P35268; Q96MF2: STAC3; NbExp=3; IntAct=EBI-354533, EBI-745680;
CC P35268; O75683: SURF6; NbExp=3; IntAct=EBI-354533, EBI-2691252;
CC P35268; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-354533, EBI-741515;
CC P35268; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-354533, EBI-597063;
CC P35268; P17473: IE; Xeno; NbExp=2; IntAct=EBI-354533, EBI-11702772;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- MISCELLANEOUS: Binds to Epstein-Barr virus small RNAs and to heparin.
CC {ECO:0000269|PubMed:1846807}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL22 family.
CC {ECO:0000305}.
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DR EMBL; X59357; CAA42007.1; -; mRNA.
DR EMBL; D17652; BAA04545.1; -; mRNA.
DR EMBL; AK311749; BAG34692.1; -; mRNA.
DR EMBL; CR456873; CAG33154.1; -; mRNA.
DR EMBL; AL031847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471130; EAW71518.1; -; Genomic_DNA.
DR EMBL; BC035566; AAH35566.1; -; mRNA.
DR EMBL; BC058887; AAH58887.1; -; mRNA.
DR EMBL; BC066314; AAH66314.1; -; mRNA.
DR CCDS; CCDS58.1; -.
DR PIR; JC2120; JC2120.
DR RefSeq; NP_000974.1; NM_000983.3.
DR PDB; 4UG0; EM; -; LU=1-128.
DR PDB; 4V6X; EM; 5.00 A; CU=1-128.
DR PDB; 5AJ0; EM; 3.50 A; AU=1-128.
DR PDB; 5LKS; EM; 3.60 A; LU=1-128.
DR PDB; 5T2C; EM; 3.60 A; O=1-128.
DR PDB; 6IP5; EM; 3.90 A; 2O=1-128.
DR PDB; 6IP6; EM; 4.50 A; 2O=1-128.
DR PDB; 6IP8; EM; 3.90 A; 2O=1-128.
DR PDB; 6LQM; EM; 3.09 A; d=1-128.
DR PDB; 6LSR; EM; 3.13 A; d=1-128.
DR PDB; 6LSS; EM; 3.23 A; d=1-128.
DR PDB; 6LU8; EM; 3.13 A; d=1-128.
DR PDB; 6OLE; EM; 3.10 A; V=18-116.
DR PDB; 6OLF; EM; 3.90 A; V=18-116.
DR PDB; 6OLG; EM; 3.40 A; AU=18-116.
DR PDB; 6OLI; EM; 3.50 A; V=18-116.
DR PDB; 6OLZ; EM; 3.90 A; AU=18-116.
DR PDB; 6OM0; EM; 3.10 A; V=18-116.
DR PDB; 6OM7; EM; 3.70 A; V=18-116.
DR PDB; 6QZP; EM; 2.90 A; LU=17-117.
DR PDB; 6W6L; EM; 3.84 A; V=1-128.
DR PDB; 6Y0G; EM; 3.20 A; LU=1-128.
DR PDB; 6Y2L; EM; 3.00 A; LU=1-128.
DR PDB; 6Y57; EM; 3.50 A; LU=1-128.
DR PDB; 6Y6X; EM; 2.80 A; LU=19-117.
DR PDB; 6Z6L; EM; 3.00 A; LU=1-128.
DR PDB; 6Z6M; EM; 3.10 A; LU=1-128.
DR PDB; 6Z6N; EM; 2.90 A; LU=1-128.
DR PDB; 6ZM7; EM; 2.70 A; LU=1-128.
DR PDB; 6ZME; EM; 3.00 A; LU=1-128.
DR PDB; 6ZMI; EM; 2.60 A; LU=1-128.
DR PDB; 6ZMO; EM; 3.10 A; LU=1-128.
DR PDB; 7BHP; EM; 3.30 A; LU=1-128.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
DR PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6W6L; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6Y6X; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 7BHP; -.
DR AlphaFoldDB; P35268; -.
DR SMR; P35268; -.
DR BioGRID; 112066; 316.
DR CORUM; P35268; -.
DR IntAct; P35268; 105.
DR MINT; P35268; -.
DR STRING; 9606.ENSP00000346088; -.
DR GlyGen; P35268; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P35268; -.
DR PhosphoSitePlus; P35268; -.
DR SwissPalm; P35268; -.
DR BioMuta; RPL22; -.
DR SWISS-2DPAGE; P35268; -.
DR EPD; P35268; -.
DR jPOST; P35268; -.
DR MassIVE; P35268; -.
DR MaxQB; P35268; -.
DR PaxDb; P35268; -.
DR PeptideAtlas; P35268; -.
DR PRIDE; P35268; -.
DR ProteomicsDB; 55018; -.
DR TopDownProteomics; P35268; -.
DR Antibodypedia; 27215; 192 antibodies from 31 providers.
DR DNASU; 6146; -.
DR Ensembl; ENST00000234875.9; ENSP00000346088.3; ENSG00000116251.11.
DR GeneID; 6146; -.
DR KEGG; hsa:6146; -.
DR MANE-Select; ENST00000234875.9; ENSP00000346088.3; NM_000983.4; NP_000974.1.
DR UCSC; uc001amd.4; human.
DR CTD; 6146; -.
DR DisGeNET; 6146; -.
DR GeneCards; RPL22; -.
DR HGNC; HGNC:10315; RPL22.
DR HPA; ENSG00000116251; Low tissue specificity.
DR MIM; 180474; gene.
DR neXtProt; NX_P35268; -.
DR OpenTargets; ENSG00000116251; -.
DR PharmGKB; PA34688; -.
DR VEuPathDB; HostDB:ENSG00000116251; -.
DR eggNOG; KOG3434; Eukaryota.
DR GeneTree; ENSGT00940000153314; -.
DR HOGENOM; CLU_105624_0_1_1; -.
DR InParanoid; P35268; -.
DR OMA; NTAISMY; -.
DR OrthoDB; 1594080at2759; -.
DR PhylomeDB; P35268; -.
DR TreeFam; TF313018; -.
DR PathwayCommons; P35268; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P35268; -.
DR SIGNOR; P35268; -.
DR BioGRID-ORCS; 6146; 341 hits in 1076 CRISPR screens.
DR ChiTaRS; RPL22; human.
DR GeneWiki; RPL22; -.
DR GenomeRNAi; 6146; -.
DR Pharos; P35268; Tbio.
DR PRO; PR:P35268; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P35268; protein.
DR Bgee; ENSG00000116251; Expressed in calcaneal tendon and 204 other tissues.
DR ExpressionAtlas; P35268; baseline and differential.
DR Genevisible; P35268; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; HDA:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0045182; F:translation regulator activity; IEA:Ensembl.
DR GO; GO:0046632; P:alpha-beta T cell differentiation; IEA:Ensembl.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0099577; P:regulation of translation at presynapse, modulating synaptic transmission; IEA:Ensembl.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR Gene3D; 3.30.1360.210; -; 1.
DR InterPro; IPR002671; Ribosomal_L22e.
DR InterPro; IPR038526; Ribosomal_L22e_sf.
DR PANTHER; PTHR10064; PTHR10064; 1.
DR Pfam; PF01776; Ribosomal_L22e; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Heparin-binding;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1846807, ECO:0000269|Ref.5"
FT CHAIN 2..128
FT /note="60S ribosomal protein L22"
FT /id="PRO_0000215501"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P67984"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 69
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P67984"
SQ SEQUENCE 128 AA; 14787 MW; 0F3ED8BE70C9F962 CRC64;
MAPVKKLVVK GGKKKKQVLK FTLDCTHPVE DGIMDAANFE QFLQERIKVN GKAGNLGGGV
VTIERSKSKI TVTSEVPFSK RYLKYLTKKY LKKNNLRDWL RVVANSKESY ELRYFQINQD
EEEEEDED
